Results 71 to 80 of about 15,262 (93)

Palmitoylated proteins

open access: yes, 2023
Triola, Gemma   +1 more
openaire   +1 more source

Palmitoylation in apoptosis

Journal of Cellular Physiology, 2023
AbstractPalmitoylation, a critical lipid modification of proteins, is involved in various physiological processes such as altering protein localization, transport, and stability, which perform essential roles in protein function. Palmitoyltransferases are specific enzymes involved in the palmitoylation modification of substrates.
Peiyao Li   +6 more
openaire   +2 more sources

Palmitoylation and palmitoyl-transferases in Plasmodium parasites [PDF]

open access: possibleBiochemical Society Transactions, 2015
Protein post-translational modifications (PTM) are commonly used to regulate biological processes. Protein S-acylation is an enzymatically regulated reversible modification that has been shown to modulate protein localization, activity and membrane binding.
Julian C. Rayner   +5 more
openaire   +2 more sources

Palmitoylation of Tubulin

Biochemical and Biophysical Research Communications, 1997
Tubulin is a very water soluble protein, yet a significant portion is firmly associated with cell membranes. Because recent work has shown that palmitoylation is a dynamic process that can alter the targeting of proteins to membranes, we tested whether or not tubulin could be palmitoylated to account for its membrane location.
J. Wolff, Anna Maria Zambito
openaire   +3 more sources

Palmitoylation, pathogens and their host

Biochemical Society Transactions, 2013
S-Palmitoylation, the only reversible post-translational lipid modification, confers unique biochemical and functional properties to proteins. Although it has long been known that viral proteins are palmitoylated, recent studies reveal that this modification plays a critical role for pathogens of all kinds and at multiple steps of their life cycle. The
Blanc Mathieu   +2 more
openaire   +3 more sources

Palmitoylation as a Signal for Delivery

2020
The ligands and receptors in immune checkpoint signaling are typically transmembrane proteins, which may be regulated by palmitoylation as a reversible lipid modification. Our recent work demonstrated that palmitoylation reduces the lysosomal degradation of PD-L1 trafficking and may present a new therapeutic target.
Caiyun Fang   +3 more
openaire   +2 more sources

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